RBP2 is essential for the proper handling of retinoids, which are vital for various physiological processes, including vision, growth, reproduction, and differentiation of epithelial tissues . Retinoids, such as retinol and retinoic acid, are forms of vitamin A that are necessary for gene expression modulation and overall embryonic development .
Studies have shown that RBP2 is not required during times of dietary retinoid sufficiency. However, in conditions of retinoid insufficiency, the absence of RBP2 can lead to perinatal lethality due to its critical role in both maternal and neonatal tissues . Additionally, RBP2-deficient mice on a high-fat diet have been observed to develop obesity, glucose intolerance, and fatty liver .
RBP2 binds retinol with high affinity, facilitating its transport and metabolism within cells . Interestingly, recent research has revealed that RBP2 also binds long-chain 2-monoacylglycerols (2-MAGs), including the endocannabinoid 2-arachidonoylglycerol, with an affinity equivalent to that of retinol . This dual binding capability suggests a broader physiological role for RBP2 beyond retinoid metabolism.
Recombinant human RBP2 is typically expressed in E. coli and has a molecular weight of approximately 15.7 kDa . It is used in research to study the protein’s function and its role in various biological processes. The recombinant protein is often lyophilized and can be stored for extended periods under appropriate conditions .